The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Ankyrin
Open accessAbstract
We have characterized a new ankyrin gene, expressed in brain and other tissues, that is subject to extensive tissue-specific alternative mRNA processing. The full-length polypeptide has a molecular mass of 480 kDa and includes a predicted globular head domain, with membrane- and spectrin-binding activities, as well as an extended "tail" domain. We term this gene ankyrinG based on its giant size and general expression. Two brain-specific isoforms of 480 kDa and 270 kDa were identified that contain a unique stretch of sequence highly enriched in serine and threonine residues immediately following the globular head domain. Antibodies against the serine-rich domain and spectrin-binding domain revealed labeling of nodes of Ranvier and axonal initial segments. Ankyrin-binding proteins also known to be localized in these specialized membrane domains include the voltage-dependent sodium channel, the sodium/potassium ATPase, sodium/calcium exchanger, and members of the neurofascin/L1 family of cell adhesion molecules. The neural-specific ankyrinG polypeptides are candidates to participate in maintenance/targeting of ion channels and cell adhesion molecules to nodes of Ranvier and axonal initial segments.
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Biology of Oligodendrocyte and Myelin in the Mammalian Central Nervous System
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Actin, Spectrin, and Associated Proteins Form a Periodic Cytoskeletal Structure in Axons
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Action potential generation requires a high sodium channel density in the axon initial segment
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Metadata
- Authors
- Kordeli, E., Lambert, S., & Bennett, V.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-02
- Volume
- 270
- Issue
- 5
- Pages
- 2352-2359
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1606121092
- Cited by
- 489
- References
- 22
- FWCI
- 6.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 9405 d)
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- Kordeli, E., Lambert, S., & Bennett, V. (1995). Ankyrin. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.5.2352
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
